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Article

Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.

Blood - 15 Sept 2004

Yang Likui, Manithody Chandrashekhara, Rezaie Alireza R

Abstract excerpt

A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin. In this study, it was hypothesized that differences in the structure of the autolysis loop of coagulation proteases (residues...

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Identifiers

PMID: 15178583
DOI: 10.1182/blood-2004-03-1092

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Heparin-activated antithrombin interacts with the autolysis loop of target coagulation proteases.PMID 15178583Read ↗

The role of autolysis loop in determining the specificity of coagulation proteases.Semantic proximity Read ↗

Allosteric activation of antithrombin critically depends upon hinge region extension.Semantic proximity Read ↗

Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin.Semantic proximity Read ↗

Heparin chain-length dependence of factor Xa inhibition by antithrombin in plasma.Semantic proximity Read ↗

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

Evolution of serpin specificity: cooperative interactions in the reactive-site loop sequence of antithrombin specifically restrict the inhibition of activated protein C.Semantic proximity Read ↗

Role of N- and C-terminal amino acids in antithrombin binding to pentasaccharide.Semantic proximity Read ↗

Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.Semantic proximity Read ↗

The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Semantic proximity Read ↗

Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties.Semantic proximity Read ↗

Crystal structure of monomeric native antithrombin reveals a novel reactive center loop conformation.Semantic proximity Read ↗

The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.Semantic proximity Read ↗

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